NUCB1_MOUSE
ID NUCB1_MOUSE Reviewed; 459 AA.
AC Q02819; Q3TU42; Q9CWA1; Q9D8J4; Q9DBL3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Nucleobindin-1;
DE AltName: Full=CALNUC;
DE Flags: Precursor;
GN Name=Nucb1; Synonyms=Nuc, Nucb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1520323; DOI=10.1016/s0006-291x(05)81503-7;
RA Miura K., Titani K., Kurosawa Y., Kanai Y.;
RT "Molecular cloning of nucleobindin, a novel DNA-binding protein that
RT contains both a signal peptide and a leucine zipper structure.";
RL Biochem. Biophys. Res. Commun. 187:375-380(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Corpus striatum, Head, Kidney, Liver, Pancreas, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION AT SER-85.
RX PubMed=15378723; DOI=10.1002/rcm.1604;
RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT purification and linear ion trap mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-368 AND SER-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Major calcium-binding protein of the Golgi which may have a
CC role in calcium homeostasis (By similarity). Acts as a non-receptor
CC guanine nucleotide exchange factor which binds to and activates alpha
CC subunits of guanine nucleotide-binding proteins (G proteins) (By
CC similarity). {ECO:0000250|UniProtKB:Q0P569,
CC ECO:0000250|UniProtKB:Q63083}.
CC -!- SUBUNIT: Interacts (via GBA motif) with guanine nucleotide-binding
CC protein G(i) alpha subunits GNAI1, GNAI2 and GNAI3 with higher affinity
CC for GNAI1 and GNAI3 than for GNAI2. Preferentially interacts with
CC inactive rather than active GNAI3. Interaction with GNAI3 is inhibited
CC when NUCB1 binds calcium, probably due to a conformational change which
CC renders the GBA motif inaccessible. {ECO:0000250|UniProtKB:Q63083}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q63083}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q63083}; Lumenal side
CC {ECO:0000250|UniProtKB:Q63083}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q63083}. Secreted
CC {ECO:0000250|UniProtKB:Q63083}. Note=A small fraction of the protein
CC may be cytoplasmic. In bone at least part of it is found in the
CC extracellular matrix and in the culture medium of calvaria explants (By
CC similarity). In lupus prone, but not in normal mice, at least part of
CC it is in the serum where it induces the formation of autoantibodies
CC including anti-DNA antibodies. {ECO:0000250|UniProtKB:Q63083,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Lymphoid cells as well as other somatic cells, such
CC as liver and kidney cells.
CC -!- DOMAIN: The EF-hand domains are unfolded in the absence of Ca(2+) and
CC fold upon Ca(2+) addition. {ECO:0000250|UniProtKB:Q02818}.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins). {ECO:0000250|UniProtKB:Q63083}.
CC -!- MISCELLANEOUS: Discovered as DNA-binding protein in the serum of lupus-
CC prone mice.
CC -!- SIMILARITY: Belongs to the nucleobindin family. {ECO:0000305}.
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DR EMBL; M96823; AAA39842.1; -; mRNA.
DR EMBL; AK002630; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK004886; BAB23644.1; -; mRNA.
DR EMBL; AK007976; BAB25383.1; -; mRNA.
DR EMBL; AK140710; BAE24451.1; -; mRNA.
DR EMBL; AK160981; BAE36129.1; -; mRNA.
DR EMBL; AK164088; BAE37619.1; -; mRNA.
DR EMBL; BC072554; AAH72554.1; -; mRNA.
DR CCDS; CCDS52247.1; -.
DR PIR; JC1224; JC1224.
DR RefSeq; NP_001157134.1; NM_001163662.1.
DR RefSeq; NP_032775.1; NM_008749.2.
DR RefSeq; XP_006540759.1; XM_006540696.2.
DR RefSeq; XP_017177513.1; XM_017322024.1.
DR AlphaFoldDB; Q02819; -.
DR BMRB; Q02819; -.
DR SMR; Q02819; -.
DR BioGRID; 201875; 23.
DR IntAct; Q02819; 4.
DR STRING; 10090.ENSMUSP00000033096; -.
DR iPTMnet; Q02819; -.
DR PhosphoSitePlus; Q02819; -.
DR CPTAC; non-CPTAC-3662; -.
DR EPD; Q02819; -.
DR jPOST; Q02819; -.
DR MaxQB; Q02819; -.
DR PaxDb; Q02819; -.
DR PeptideAtlas; Q02819; -.
DR PRIDE; Q02819; -.
DR ProteomicsDB; 287845; -.
DR Antibodypedia; 2173; 306 antibodies from 30 providers.
DR DNASU; 18220; -.
DR Ensembl; ENSMUST00000211765; ENSMUSP00000147383; ENSMUSG00000030824.
DR GeneID; 18220; -.
DR KEGG; mmu:18220; -.
DR UCSC; uc009gvm.2; mouse.
DR CTD; 4924; -.
DR MGI; MGI:97388; Nucb1.
DR VEuPathDB; HostDB:ENSMUSG00000030824; -.
DR eggNOG; KOG3866; Eukaryota.
DR GeneTree; ENSGT00390000001927; -.
DR HOGENOM; CLU_031153_1_0_1; -.
DR InParanoid; Q02819; -.
DR OMA; QETDTNH; -.
DR OrthoDB; 1445357at2759; -.
DR PhylomeDB; Q02819; -.
DR TreeFam; TF323218; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 18220; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Nucb1; mouse.
DR PRO; PR:Q02819; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q02819; protein.
DR Bgee; ENSMUSG00000030824; Expressed in prostate gland ventral lobe and 262 other tissues.
DR ExpressionAtlas; Q02819; baseline and differential.
DR Genevisible; Q02819; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0090498; C:extrinsic component of Golgi membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; ISO:MGI.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR GO; GO:0098547; C:lumenal side of Golgi membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:1903533; P:regulation of protein targeting; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR040253; NUCB1.
DR InterPro; IPR040250; Nucleobindin.
DR PANTHER; PTHR19237; PTHR19237; 1.
DR PANTHER; PTHR19237:SF21; PTHR19237:SF21; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250|UniProtKB:Q0P569"
FT CHAIN 26..459
FT /note="Nucleobindin-1"
FT /id="PRO_0000004163"
FT DOMAIN 239..274
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 291..326
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DNA_BIND 171..217
FT /evidence="ECO:0000255"
FT REGION 192..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..320
FT /note="Binds to GNAI2 and GNAI3"
FT /evidence="ECO:0000250"
FT REGION 368..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..217
FT /evidence="ECO:0000255"
FT COILED 340..407
FT /evidence="ECO:0000255"
FT MOTIF 302..332
FT /note="GBA"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT COMPBIAS 192..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15378723,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02818"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 42
FT /note="E -> D (in Ref. 2; BAB25383)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="H -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="R -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 390..393
FT /note="Missing (in Ref. 1; AAA39842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 53409 MW; 1CC1102D216CC60B CRC64;
MPTSVPRGAP FLLLPPLLML SAVLAVPVDR AAPPQEDSQA TETPDTGLYY HRYLQEVINV
LETDGHFREK LQAANAEDIK SGKLSQELDF VSHNVRTKLD ELKRQEVSRL RMLLKAKMDA
KQEPNLQVDH MNLLKQFEHL DPQNQHTFEA RDLELLIQTA TRDLAQYDAA HHEEFKRYEM
LKEHERRRYL ESLGEEQRKE AERKLQEQQR RHREHPKVNV PGSQAQLKEV WEELDGLDPN
RFNPKTFFIL HDINSDGVLD EQELEALFTK ELEKVYDPKN EEDDMREMEE ERLRMREHVM
KNVDTNQDRL VTLEEFLAST QRKEFGDTGE GWKTVEMSPA YTEEELKRFE EELAAREAEL
NARAQRLSQE TEALGRSQDR LEAQKRELQQ AVLQMEQRKQ QLQEQSAPPS KPDGQLQFRA
DTDDAPVPAP AGDQKDVPAS EKKVPEQPPE LPQLDSQHL
